The raw starch binding domain of cyclodextrin glycosyltransferase from Bacillus circulans strain 251
about
The cyclization mechanism of cyclodextrin glycosyltransferase (CGTase) as revealed by a gamma-cyclodextrin-CGTase complex at 1.8-A resolutionThe remote substrate binding subsite -6 in cyclodextrin-glycosyltransferase controls the transferase activity of the enzyme via an induced-fit mechanismThe fully conserved Asp residue in conserved sequence region I of the alpha-amylase family is crucial for the catalytic site architecture and activityThe 'pair of sugar tongs' site on the non-catalytic domain C of barley alpha-amylase participates in substrate binding and activityStarch Catabolism by a Prominent Human Gut Symbiont Is Directed by the Recognition of Amylose HelicesMultidomain Carbohydrate-binding Proteins Involved in Bacteroides thetaiotaomicron Starch MetabolismCrystal Structure of Circular Permuted RoCBM21 (CP90): Dimerisation and Proximity of Binding SitesAssociation of Novel Domain in Active Site of Archaic Hyperthermophilic Maltogenic Amylase from Staphylothermus marinusStructural Elucidation of the Cyclization Mechanism of -1,6-Glucan by Bacillus circulans T-3040 Cycloisomaltooligosaccharide GlucanotransferaseA CBM20 low-affinity starch-binding domain from glucan, water dikinase.Characteristics of two forms of alpha-amylases and structural implication.Functional demonstrations of starch binding domains present in Ostreococcus tauri starch synthases isoforms.Carbohydrate-binding module 74 is a novel starch-binding domain associated with large and multidomain α-amylase enzymes.Multigene disruption in undomesticated Bacillus subtilis ATCC 6051a using the CRISPR/Cas9 system.Unique carbohydrate binding platforms employed by the glucan phosphatases.The evolution of cyclodextrin glucanotransferase product specificity.The carbohydrate-binding module family 20--diversity, structure, and function.Microbial glucoamylases: characteristics and applications.Engineering of cyclodextrin glucanotransferases and the impact for biotechnological applications.High-level extracellular protein production in Bacillus subtilis using an optimized dual-promoter expression system.α-Amylase: an enzyme specificity found in various families of glycoside hydrolases.The role of arginine 47 in the cyclization and coupling reactions of cyclodextrin glycosyltransferase from Bacillus circulans strain 251 implications for product inhibition and product specificity.The three transglycosylation reactions catalyzed by cyclodextrin glycosyltransferase from Bacillus circulans (strain 251) proceed via different kinetic mechanisms.The starch-binding capacity of the noncatalytic SBD2 region and the interaction between the N- and C-terminal domains are involved in the modulation of the activity of starch synthase III from Arabidopsis thaliana.Structure and function of α-glucan debranching enzymes.A trehalose-6-phosphate synthase gene from Saccharina japonica (Laminariales, Phaeophyceae).Identification, cloning, expression, and characterization of the extracellular acarbose-modifying glycosyltransferase, AcbD, from Actinoplanes sp. strain SE50.Analysis of DNA binding and transcriptional activation by the LysR-type transcriptional regulator CbbR of Xanthobacter flavus.Starch-binding domain affects catalysis in two Lactobacillus alpha-amylasesA CGTase with high coupling activity using γ-cyclodextrin isolated from a novel strain clustering under the genus Carboxydocella.The cyclodextrin glycosyltransferase of Paenibacillus pabuli US132 strain: molecular characterization and overproduction of the recombinant enzyme.The unique branching patterns of Deinococcus glycogen branching enzymes are determined by their N-terminal domains.Hydrophobic amino acid residues in the acceptor binding site are main determinants for reaction mechanism and specificity of cyclodextrin-glycosyltransferase.Mutations converting cyclodextrin glycosyltransferase from a transglycosylase into a starch hydrolase.Halotolerant, acid-alkali stable, chelator resistant and raw starch digesting α-amylase from a marine bacterium Bacillus subtilis S8-18.Glucoamylase structural, functional, and evolutionary relationships.The unique evolution of the carbohydrate-binding module CBM20 in laforin.Fusion of a family 20 carbohydrate-binding module (CBM20) with cyclodextrin glycosyltransferase of Geobacillus sp. CHB1 improves catalytic efficiency.The starch-binding domain family CBM41-An in silico analysis of evolutionary relationships.Fungal lytic polysaccharide monooxygenases bind starch and β-cyclodextrin similarly to amylolytic hydrolases.
P2860
Q27620493-D473E8D0-3D00-4452-A2E5-0430213A3382Q27636015-BBF6EA3C-C51E-495C-A78E-5D9BD7441CD9Q27641036-8041D8EE-E1EA-4E8F-B0BA-A8FB571D022BQ27647824-082F3238-F22C-42A8-97A3-DC261C4417C4Q27651083-CBFE943A-D704-4305-95CF-E4C528B636AFQ27671644-482D12A9-B463-4999-B283-98FF73E1C3B8Q27675431-285A794D-A3C8-4ACC-810A-3BFF568A6BCDQ27676602-274A8320-B490-42D7-83E8-5BD1E292A018Q27682073-738ECD3B-74A7-4BEC-B5FA-7BFE43866668Q33416640-9C46A1AC-2556-48FF-9E50-EB7205076A78Q33985843-4D80CBE5-5CF7-4CEF-9E9E-E891084E52D0Q35824960-7C3045CC-D051-4DA7-97D1-BDBCEE9C12EEQ35996400-2E850875-7AEE-4E9F-BF99-F4FAF88DD29FQ37010409-E08EF64C-456D-4430-A77D-072CB03B2AFBQ37037323-0409BD57-1FAF-4C1E-8B65-130F67C5BEFFQ37271654-16B71121-6F32-4AEF-B52A-6E44DAB61A79Q37580015-3551CB14-F4C9-40DE-A439-F30132BE6E10Q37587214-8B1F50F0-388D-4908-AE38-E5F1ADB01347Q37599536-AED6784B-5353-4535-BC21-90E64A890658Q37655413-05D7984E-6F7F-457B-917E-54B68C3A653EQ38117539-9EC38D26-120B-436F-A307-7198CDCE0234Q38311498-9BBED37D-CE9B-4A5F-9DB6-C77B1911B375Q38316000-7D9647C8-4CDF-49FF-8045-8F5D5F0473E4Q38348233-1575C096-E289-4515-B620-A37656DBE7FDQ38823309-50FA3B21-8AB3-4EED-BADE-521DC5AE2151Q38970188-DEF2B911-BCF7-43BC-991C-778FBD409CABQ39504326-1E98ECE6-8A4D-4E6F-B403-326B84E37A5CQ39705936-EBDC0FB0-8FC3-494B-B93A-9593313906A6Q40898878-E8E68A00-99E9-4BAF-A178-45C588658CA1Q41684817-E4849C4D-B3F6-4D2F-810C-4B3F6912A72EQ41829361-E6CEFA49-4B47-439F-91B4-51A90E7B94B4Q42121276-FF19EAAC-695B-4BB4-898E-31ACED3CE935Q43736489-A29BF087-EF00-47C9-9BCA-89B1932BF388Q43953801-35E811FB-00AB-453D-9852-E3D95F1A79AAQ46534949-8E8CBF36-3607-41C2-A0A6-F5E971957215Q46719735-40803A52-135C-48C6-AD58-82088DA34EACQ47693014-3997BBA7-E59E-4BB4-8490-823A45CC61EBQ48063389-44C49EFC-CAEA-4244-86BB-EA07553B7A8CQ48254745-2BE7F37E-34DC-47CF-A902-318E6EA76CD6Q48555811-41079A52-AEC0-4FAD-8A7F-57B18CC59EF1
P2860
The raw starch binding domain of cyclodextrin glycosyltransferase from Bacillus circulans strain 251
description
1996 nî lūn-bûn
@nan
1996 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1996 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
1996年の論文
@ja
1996年学术文章
@wuu
1996年学术文章
@zh-cn
1996年学术文章
@zh-hans
1996年学术文章
@zh-my
1996年学术文章
@zh-sg
1996年學術文章
@yue
name
The raw starch binding domain ...... Bacillus circulans strain 251
@ast
The raw starch binding domain ...... Bacillus circulans strain 251
@en
The raw starch binding domain ...... Bacillus circulans strain 251
@nl
type
label
The raw starch binding domain ...... Bacillus circulans strain 251
@ast
The raw starch binding domain ...... Bacillus circulans strain 251
@en
The raw starch binding domain ...... Bacillus circulans strain 251
@nl
prefLabel
The raw starch binding domain ...... Bacillus circulans strain 251
@ast
The raw starch binding domain ...... Bacillus circulans strain 251
@en
The raw starch binding domain ...... Bacillus circulans strain 251
@nl
P2093
P2860
P3181
P356
P1476
The raw starch binding domain ...... Bacillus circulans strain 251
@en
P2093
B A van der Veen
B W Dijkstra
D Penninga
R M Knegtel
S A van Hijum
P2860
P304
32777-32784
P3181
P356
10.1074/JBC.271.51.32777
P407
P577
1996-12-01T00:00:00Z